Isolation and characterization of the gene coding for human cytidine deaminase.
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Demontis S, Terao M, Brivio M, Zanotta S, Bruschi M, Garattini E
Isolation and characterization of the gene coding for human cytidine deaminase.
Biochim Biophys Acta. 1998 Dec 22;1443(3):323-33.
- PubMed ID
- 9878810 [ View in PubMed]
- Abstract
The human gene coding for cytidine deaminase (CD), the enzyme which catalyzes the deamination of cytidine and deoxycytidine to uridine and deoxyuridine, was isolated and structurally characterized. CD is a single copy gene with a length of 31 kb and consists of four exons. Exon-intron junctions do not bracket functional domains of the encoded protein as the boundary between exons 2 and 3 interrupts the catalytically important zinc-finger domain, which is well conserved along phylogenesis. 5'-RACE and RNase mapping experiments identify one major and multiple other minor transcription initiation sites, which are present in placenta as well as in the myeloid cell lines, HL-60 and U937. The 5'-flanking region of the gene contains an orientation-dependent functional promoter and is characterized by the presence of several potential sites for the binding of known transcriptional factors.